1F0V: Crystal Structure Of An Rnase A Dimer Displaying A New Type Of 3d Domain Swapping

Bovine pancreatic ribonuclease (RNase A) forms two types of dimers (a major and a minor component) upon concentration in mild acid. These two dimers exhibit different biophysical and biochemical properties. Earlier we reported that the minor dimer forms by swapping its N-terminal alpha-helix with that of an identical molecule. Here we find that the major dimer forms by swapping its C-terminal beta-strand, thus revealing the first example of three-dimensional (3D) domain swapping taking place in different parts of the same protein. This feature permits RNase A to form tightly bonded higher oligomers. The hinge loop of the major dimer, connecting the swapped beta-strand to the protein core, resembles a short segment of the polar zipper proposed by Perutz and suggests a model for aggregate formation by 3D domain swapping with a polar zipper.
PDB ID: 1F0VDownload
MMDB ID: 72028
PDB Deposition Date: 2000/5/17
Updated in MMDB: 2011/06
Experimental Method:
x-ray diffraction
Resolution: 1.7  Å
Source Organism:
synthetic construct
Similar Structures:
Biological Unit for 1F0V: dimeric; determined by author
Molecular Components in 1F0V
Label Count Molecule
Protein (1 molecule)
Ribonuclease a(Gene symbol: RNASE1)
Molecule annotation
Nucleotide(1 molecule)
Molecule annotation
Chemicals (10 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB